Evidence map›Paper›PMID 25807192›Full record

ArticleScientific reports2015

Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells.

Ariadna Grau-Campistany, Erik Strandberg, Parvesh Wadhwani, Johannes Reichert, Jochen Bürck, Francesc Rabanal, Anne S Ulrich

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Article
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  9. Article
  10. Predicting Membrane-Active Peptide Dynamics in Fluidic Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Phosphate-dependent aggregation of [KL]Scientific reports · 2020
    Article
  16. Article
  17. Article
  18. A How-To Guide for Mode of Action Analysis of Antimicrobial Peptides.Frontiers in cellular and infection microbiology · 2020
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Ariadna Grau-CampistanyUniversity of Barcelona, Faculty of Chemistry, Department of Organic Chemistry, Martí i Franquès, 1, 08028, Barcelona, Spain.
Erik StrandbergKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany.
Parvesh WadhwaniKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany.
Johannes ReichertKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany.
Jochen BürckKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany.
Francesc RabanalUniversity of Barcelona, Faculty of Chemistry, Department of Organic Chemistry, Martí i Franquès, 1, 08028, Barcelona, Spain.
Anne S Ulrich1] Karlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany [2] KIT, Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrophobic mismatch is a well-recognized principle in the interaction of transmembrane proteins with lipid bilayers. This concept was extended here to amphipathic membranolytic α-helices. Nine peptides with lengths between 14 and 28 amino acids were designed from repeated KIAGKIA motifs, and their helical nature was confirmed by circular dichroism spectroscopy. Biological assays for antimicrobial activity and hemolysis, as well as fluorescence vesicle leakage and solid-state NMR spectroscopy, were used to correlate peptide length with membranolytic activity. These data show that the formation of transmembrane pores is only possible under the condition of hydrophobic matching: the peptides have to be long enough to span the hydrophobic bilayer core to be able to induce vesicle leakage, kill bacteria, and cause hemolysis. By correlating the threshold lengths for biological activity with the biophysical results on model vesicles, the peptides could be utilized as molecular rulers to measure the membrane thickness in different cells.

Indexed as

Circular DichroismEscherichia coliHydrophobic and Hydrophilic InteractionsLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsPeptidesProtein ConformationLipid BilayersMembrane ProteinsPeptides

Identifiers

PMID25807192
PMCPMC5224518

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.